About: Identification of two mutation sites in spike and envelope proteins mediating optimal cellular infection of porcine epidemic diarrhea virus from different pathways

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About: Identification of two mutation sites in spike and envelope proteins mediating optimal cellular infection of porcine epidemic diarrhea virus from different pathways Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Identification of two mutation sites in spike and envelope proteins mediating optimal cellular infection of porcine epidemic diarrhea virus from different pathways
Creator	Lu, Chengping Ma, Jiale Pan, Zihao Sun, Min Yao, Huochun Yu, Zeyanqiu
Source	Medline; PMC
abstract	Entry of the α-coronavirus porcine epidemic diarrhea virus (PEDV) requires specific proteases to activate spike (S) protein for the membrane fusion of the virion to the host cell following receptor binding. Herein, PEDV isolate 85-7 could proliferate and induce cell–cell fusion in a trypsin independent manner on Vero cells, and eight homologous mutation strains were screened by continuous proliferation in the absence of trypsin on Vero cells. According to the whole genome sequence comparative analysis, we identified four major variations located in nonstructural protein 2, S, open reading frame 3, and envelope (E) genes, respectively. Comparative analyses of their genomic variations and proliferation characteristics identified a single mutation within the S2′ cleavage site between C30 and C40 mutants: the substitution of conserved arginine (R) by a glycine (G) (R895G). This change resulted in weaker cell–cell fusion, smaller plaque morphology, higher virus titer and serious microfilament condensation. Further analysis confirmed that this mutation was responsible for optimal cell-adaptation, but not the determinant for trypsin-dependent entry of PEDV. Otherwise, a novel variation (16–20 aa deletion and an L25P mutation) in the transmembrane domain of the E protein affected multiple infection processes, including up-regulation of the production of the ER stress indicator GRP78, improving the expression of pro-inflammatory cytokines IL-6 and IL-8, and promoting apoptosis. The results of this study provide a better understanding of the potential mechanisms of viral functional proteins in PEDV replication, infection, and fitness. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13567-017-0449-y) contains supplementary material, which is available to authorized users.
has issue date	2017-08-30(xsd:dateTime)
bibo:doi	10.1186/s13567-017-0449-y
bibo:pmid	28854955
has license	cc-by
sha1sum (hex)	6a0f7cfb9306380e01f35d7f8c0e75c0f91dcbc4
schema:url	https://doi.org/10.1186/s13567-017-0449-y
resource representing a document's title	Identification of two mutation sites in spike and envelope proteins mediating optimal cellular infection of porcine epidemic diarrhea virus from different pathways
has PubMed Central identifier	PMC5577753
has PubMed identifier	28854955
schema:publication	Vet Res
resource representing a document's body	covid:6a0f7cfb9306380e01f35d7f8c0e75c0f91dcbc4#body_text
is schema:about of	named entity 'cells' named entity 'C30' named entity 'infection' named entity 'continuous' named entity 'provide' named entity 'arginine' named entity 'Vero' named entity 'envelope' named entity 'morphology' named entity 'microfilament' named entity 'trypsin' named entity 'optimal' named entity 'Identification' named entity 'COMPARATIVE' named entity 'INFECTION' named entity 'MUTATION' named entity 'UNDERSTANDING' named entity 'ANALYSIS' named entity 'GENES' named entity 'PLAQUE' named entity 'FOLLOWING' named entity 'VARIATION' named entity 'GENOMIC' named entity 'OPEN READING FRAME' named entity 'STRESS INDICATOR' named entity 'ACCORDING' named entity 'PROMOTING' named entity 'VIRION' named entity 'PROCESSES' named entity 'CLEAVAGE' named entity 'HOST CELL' named entity 'REPLICATION' named entity 'MORPHOLOGY' named entity 'APOPTOSIS' named entity 'CONDENSATION' named entity 'E PROTEIN' named entity 'CONSERVED' named entity 'IDENTIFIED' named entity 'PRODUCTION' named entity 'INDUCE' named entity 'CELL-CELL FUSION' named entity 'VIRAL' named entity 'PROTEINS' named entity 'UP-REGULATION' named entity 'MUTANTS' named entity 'SINGLE' named entity 'PORCINE EPIDEMIC DIARRHEA VIRUS' named entity 'RESPONSIBLE' named entity 'THEIR' named entity 'NOVEL' named entity 'DETERMINANT' named entity 'STRAINS' named entity 'HOMOLOGOUS' named entity '28G' named entity 'BETTER' named entity 'IMPROVING' named entity 'ABSENCE OF' named entity 'ENTRY' named entity 'MULTIPLE INFECTION' named entity 'SPIKE' named entity 'CHARACTERISTICS' named entity 'PRO-' named entity 'CONTINUOUS' named entity 'SUBSTITUTION' named entity 'TRANSMEMBRANE DOMAIN' named entity 'CHANGE' named entity 'CONFIRMED' named entity 'PATHWAYS' named entity 'OPTIMAL' named entity 'ISOLATE' named entity 'DELETION' named entity 'C40' named entity 'AFFECTED' named entity 'STUDY' named entity 'WHOLE GENOME' named entity 'SITE'

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